First evidence of a membrane-bound, tyramine and b-phenylethylamine producing, tyrosine decarboxylase in Enterococcus faecalis: A two-dimensional electrophoresis proteomic study (Articolo in rivista)

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  • First evidence of a membrane-bound, tyramine and b-phenylethylamine producing, tyrosine decarboxylase in Enterococcus faecalis: A two-dimensional electrophoresis proteomic study (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/pmic.200800780 (literal)
Alternative label
  • Enrica Pessione 1, Alessandro Pessione 1, Cristina Lamberti 1, Daniel Jean Co?sson 2, Kathrin Riedel 3, Roberto Mazzoli 1, Silvia Bonetta 4, Leo Eberl 3 and Carlo Giunta 1 (2009)
    First evidence of a membrane-bound, tyramine and b-phenylethylamine producing, tyrosine decarboxylase in Enterococcus faecalis: A two-dimensional electrophoresis proteomic study
    in Proteomics (Weinh., Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Enrica Pessione 1, Alessandro Pessione 1, Cristina Lamberti 1, Daniel Jean Co?sson 2, Kathrin Riedel 3, Roberto Mazzoli 1, Silvia Bonetta 4, Leo Eberl 3 and Carlo Giunta 1 (literal)
Pagina inizio
  • 1 (literal)
Pagina fine
  • 16 (literal)
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  • 9 (literal)
Rivista
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  • 1 Dipartimento di Biologia Animale e dell'Uomo, University of Torino, Torino, Italy 2 DISCAFF, University of Piemonte Orientale ''A.Avogadro'', Novara, Italy 3 Institute of Plant Biology, Department of Microbiology, University of Zurich, Zurich, Switzerland 4 Dipartimento di Scienze dell'Ambiente e della Vita, University of Piemonte Orientale ''A.Avogadro'',Alessandria, Italy (literal)
Titolo
  • First evidence of a membrane-bound, tyramine and b-phenylethylamine producing, tyrosine decarboxylase in Enterococcus faecalis: A two-dimensional electrophoresis proteomic study (literal)
Abstract
  • The soluble and membrane proteome of a tyramine producing Enterococcus faecalis, isolated from an Italian goat cheese, was investigated. A detailed analysis revealed that this strain also produces small amounts of b-phenylethylamine. Kinetics of tyramine and b-phenylethyla- mine accumulation, evaluated in tyrosine plus phenylalanine-enriched cultures (stimulated condition), suggest that the same enzyme, the tyrosine decarboxylase (TDC), catalyzes both tyrosine and phenylalanine decarboxylation: tyrosine was recognized as the first substrate and completely converted into tyramine (100% yield) while phenylalanine was decarboxylated to b-phenylethylamine (10% yield) only when tyrosine was completely depleted. The presence of an aspecific aromatic amino acid decarboxylase is a common feature in eukaryotes, but in bacteria only indirect evidences of a phenylalanine decarboxylating TDC have been presented so far. Comparative proteomic investigations, performed by 2-DE and MALDI-TOF/TOF MS, on bacteria grown in conditions stimulating tyramine and b-phenylethylamine biosynthesis and in control conditions revealed 49 differentially expressed proteins. Except for aromatic amino acid biosynthetic enzymes, no significant down-regulation of the central metabolic pathways was observed in stimulated conditions, suggesting that tyrosine decarboxylation does not compete with the other energy-supplying routes. The most interesting finding is a membrane-bound TDC highly over-expressed during amine production. This is the first evidence of a true membrane-bound TDC, longly suspected in bacteria on the basis of the gene sequence. (literal)
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